SAB3500884
Monoclonal Anti-HIV-1 P24-Biotin antibody produced in mouse
clone 8G9, affinity isolated antibody
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About This Item
Recommended Products
conjugate
biotin conjugate
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
8G9, monoclonal
form
buffered aqueous solution
species reactivity
virus
concentration
1 mg/mL
technique(s)
ELISA: suitable
immunoblotting: suitable
NCBI accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Immunogen
Antibody was raised against a recombinant full-length HIV-1 p24 protein.
Features and Benefits
Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.
Physical form
Supplied at 1 mg/mL in PBS with 0.02% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Proceedings of the National Academy of Sciences of the United States of America, 108(17), 7131-7136 (2011-04-07)
Protein vaccines, if rendered immunogenic, would facilitate vaccine development against HIV and other pathogens. We compared in nonhuman primates (NHPs) immune responses to HIV Gag p24 within 3G9 antibody to DEC205 ("DEC-HIV Gag p24"), an uptake receptor on dendritic cells
Micron (Oxford, England : 1993), 29(2-3), 123-138 (1998-07-31)
The life-cycle of human immunodeficiency virus type 1 (HIV-1) has been studied using several techniques including immunoelectron microscopy and cryomicroscopy. The HIV-1 particle consists of an envelope, a core and the region between the core and the envelope (matrix). Virus
Virology, 251(1), 1-15 (1998-11-14)
The Gag proteins of HIV-1, like those of other retroviruses, are necessary and sufficient for the assembly of virus-like particles. The roles played by HIV-1 Gag proteins during the life cycle are numerous and complex, involving not only assembly but
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